ADT1_MOUSE
ID ADT1_MOUSE Reviewed; 298 AA.
AC P48962; Q62164;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=ADP/ATP translocase 1 {ECO:0000305};
DE AltName: Full=ADP,ATP carrier protein 1 {ECO:0000303|PubMed:31341297};
DE AltName: Full=ADP,ATP carrier protein, heart/skeletal muscle isoform T1 {ECO:0000250|UniProtKB:P12235};
DE AltName: Full=Adenine nucleotide translocator 1 {ECO:0000303|PubMed:8903724};
DE Short=ANT 1 {ECO:0000303|PubMed:8903724};
DE AltName: Full=Solute carrier family 25 member 4 {ECO:0000305};
GN Name=Slc25a4 {ECO:0000312|MGI:MGI:1353495};
GN Synonyms=Aac1 {ECO:0000303|PubMed:31341297}, Anc1,
GN Ant1 {ECO:0000303|PubMed:8903724};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=8903724; DOI=10.1007/s003359900007;
RA Ellison J.W., Li X., Francke U., Shapiro L.J.;
RT "Rapid evolution of human pseudoautosomal genes and their mouse homologs.";
RL Mamm. Genome 7:25-30(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=BALB/cJ; TISSUE=Muscle;
RA Laplace C., Costet P.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10974536; DOI=10.1016/s0378-1119(00)00252-3;
RA Levy S.E., Chen Y.-S., Graham B.H., Wallace D.C.;
RT "Expression and sequence analysis of the mouse adenine nucleotide
RT translocase 1 and 2 genes.";
RL Gene 254:57-66(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 81-92, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=9207786; DOI=10.1038/ng0797-226;
RA Graham B.H., Waymire K.G., Cottrell B., Trounce I.A., MacGregor G.R.,
RA Wallace D.C.;
RT "A mouse model for mitochondrial myopathy and cardiomyopathy resulting from
RT a deficiency in the heart/muscle isoform of the adenine nucleotide
RT translocator.";
RL Nat. Genet. 16:226-234(1997).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH ARL2 AND ARL2BP, INTERACTION WITH ARL2BP,
RP AND TISSUE SPECIFICITY.
RX PubMed=11809823; DOI=10.1091/mbc.01-05-0245;
RA Sharer J.D., Shern J.F., Van Valkenburgh H., Wallace D.C., Kahn R.A.;
RT "ARL2 and BART enter mitochondria and bind the adenine nucleotide
RT transporter.";
RL Mol. Biol. Cell 13:71-83(2002).
RN [8]
RP DISRUPTION PHENOTYPE.
RX PubMed=14749836; DOI=10.1038/nature02229;
RA Kokoszka J.E., Waymire K.G., Levy S.E., Sligh J.E., Cai J., Jones D.P.,
RA MacGregor G.R., Wallace D.C.;
RT "The ADP/ATP translocator is not essential for the mitochondrial
RT permeability transition pore.";
RL Nature 427:461-465(2004).
RN [9]
RP DISRUPTION PHENOTYPE.
RX PubMed=16303948; DOI=10.1167/iovs.05-0695;
RA Yin H., Stahl J.S., Andrade F.H., McMullen C.A., Webb-Wood S., Newman N.J.,
RA Biousse V., Wallace D.C., Pardue M.T.;
RT "Eliminating the Ant1 isoform produces a mouse with CPEO pathology but
RT normal ocular motility.";
RL Invest. Ophthalmol. Vis. Sci. 46:4555-4562(2005).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [11]
RP TRANSGLUTAMINATION, INTERACTION WITH TGM2, AND SUBCELLULAR LOCATION.
RX PubMed=19644512; DOI=10.1038/cdd.2009.100;
RA Malorni W., Farrace M.G., Matarrese P., Tinari A., Ciarlo L.,
RA Mousavi-Shafaei P., D'Eletto M., Di Giacomo G., Melino G., Palmieri L.,
RA Rodolfo C., Piacentini M.;
RT "The adenine nucleotide translocator 1 acts as a type 2 transglutaminase
RT substrate: implications for mitochondrial-dependent apoptosis.";
RL Cell Death Differ. 16:1480-1492(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [13]
RP DISRUPTION PHENOTYPE.
RX PubMed=20671283; DOI=10.1167/iovs.10-5421;
RA Phillips M.J., Webb-Wood S., Faulkner A.E., Jabbar S.B., Biousse V.,
RA Newman N.J., Do V.T., Boatright J.H., Wallace D.C., Pardue M.T.;
RT "Retinal function and structure in Ant1-deficient mice.";
RL Invest. Ophthalmol. Vis. Sci. 51:6744-6752(2010).
RN [14]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-147; LYS-245 AND LYS-272, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast, and Liver;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [15]
RP FUNCTION, DISRUPTION PHENOTYPE, AND TISSUE SPECIFICITY.
RX PubMed=31489369; DOI=10.1126/sciadv.aaw4597;
RA Karch J., Bround M.J., Khalil H., Sargent M.A., Latchman N., Terada N.,
RA Peixoto P.M., Molkentin J.D.;
RT "Inhibition of mitochondrial permeability transition by deletion of the ANT
RT family and CypD.";
RL Sci. Adv. 5:eaaw4597-eaaw4597(2019).
RN [16]
RP FUNCTION, DISRUPTION PHENOTYPE, INTERACTION WITH TIMM44, AND MUTAGENESIS OF
RP LYS-43; ALA-90; ALA-123; 146-GLY-LYS-147 AND ARG-244.
RX PubMed=31618756; DOI=10.1038/s41586-019-1667-4;
RA Hoshino A., Wang W.J., Wada S., McDermott-Roe C., Evans C.S., Gosis B.,
RA Morley M.P., Rathi K.S., Li J., Li K., Yang S., McManus M.J., Bowman C.,
RA Potluri P., Levin M., Damrauer S., Wallace D.C., Holzbaur E.L.F., Arany Z.;
RT "The ADP/ATP translocase drives mitophagy independent of nucleotide
RT exchange.";
RL Nature 575:375-379(2019).
RN [17]
RP FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY REGULATION, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=31341297; DOI=10.1038/s41586-019-1400-3;
RA Bertholet A.M., Chouchani E.T., Kazak L., Angelin A., Fedorenko A.,
RA Long J.Z., Vidoni S., Garrity R., Cho J., Terada N., Wallace D.C.,
RA Spiegelman B.M., Kirichok Y.;
RT "H+ transport is an integral function of the mitochondrial ADP/ATP
RT carrier.";
RL Nature 571:515-520(2019).
CC -!- FUNCTION: ADP:ATP antiporter that mediates import of ADP into the
CC mitochondrial matrix for ATP synthesis, and export of ATP out to fuel
CC the cell (PubMed:31618756, PubMed:31341297). Cycles between the
CC cytoplasmic-open state (c-state) and the matrix-open state (m-state):
CC operates by the alternating access mechanism with a single substrate-
CC binding site intermittently exposed to either the cytosolic (c-state)
CC or matrix (m-state) side of the inner mitochondrial membrane (By
CC similarity). In addition to its ADP:ATP antiporter activity, also
CC involved in mitochondrial uncoupling and mitochondrial permeability
CC transition pore (mPTP) activity (PubMed:31489369, PubMed:31341297).
CC Plays a role in mitochondrial uncoupling by acting as a proton
CC transporter: proton transport uncouples the proton flows via the
CC electron transport chain and ATP synthase to reduce the efficiency of
CC ATP production and cause mitochondrial thermogenesis (PubMed:31341297).
CC Proton transporter activity is inhibited by ADP:ATP antiporter
CC activity, suggesting that SLC25A4/ANT1 acts as a master regulator of
CC mitochondrial energy output by maintaining a delicate balance between
CC ATP production (ADP:ATP antiporter activity) and thermogenesis (proton
CC transporter activity) (PubMed:31341297). Proton transporter activity
CC requires free fatty acids as cofactor, but does not transport it
CC (PubMed:31341297). Probably mediates mitochondrial uncoupling in
CC tissues that do not express UCP1 (PubMed:31341297). Also plays a key
CC role in mPTP opening, a non-specific pore that enables free passage of
CC the mitochondrial membranes to solutes of up to 1.5 kDa, and which
CC contributes to cell death (PubMed:31489369). It is however unclear if
CC SLC25A4/ANT1 constitutes a pore-forming component of mPTP or regulates
CC it (PubMed:31489369). Acts as a regulator of mitophagy independently of
CC ADP:ATP antiporter activity: promotes mitophagy via interaction with
CC TIMM44, leading to inhibit the presequence translocase TIMM23, thereby
CC promoting stabilization of PINK1 (PubMed:31618756).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000269|PubMed:31341297,
CC ECO:0000269|PubMed:31489369, ECO:0000269|PubMed:31618756}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000269|PubMed:31341297};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) = H(+)(out); Xref=Rhea:RHEA:34979, ChEBI:CHEBI:15378;
CC Evidence={ECO:0000269|PubMed:31341297};
CC -!- ACTIVITY REGULATION: The matrix-open state (m-state) is inhibited by
CC the membrane-permeable bongkrekic acid (BKA) (By similarity). The
CC cytoplasmic-open state (c-state) is inhibited by the membrane-
CC impermeable toxic inhibitor carboxyatractyloside (CATR) (By
CC similarity). Proton transporter activity is inhibited by ADP:ATP
CC antiporter activity (PubMed:31341297). {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000269|PubMed:31341297}.
CC -!- SUBUNIT: Monomer (By similarity). Found in a complex with ARL2, ARL2BP
CC and SLC25A4/ANT1 (PubMed:11809823). Interacts with ARL2BP
CC (PubMed:11809823). Interacts with TIMM44; leading to inhibit the
CC presequence translocase TIMM23, thereby promoting stabilization of
CC PINK1 (PubMed:31618756). {ECO:0000250|UniProtKB:G2QNH0,
CC ECO:0000250|UniProtKB:P02722, ECO:0000269|PubMed:11809823,
CC ECO:0000269|PubMed:31618756}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000305|PubMed:19644512}; Multi-pass membrane protein
CC {ECO:0000255}. Membrane {ECO:0000250|UniProtKB:P12235}; Multi-pass
CC membrane protein {ECO:0000255}. Note=The complex formed with ARL2BP,
CC ARL2 and SLC25A4/ANT1 is expressed in mitochondria (PubMed:11809823).
CC May localize to non-mitochondrial membranes (By similarity).
CC {ECO:0000250|UniProtKB:P12235, ECO:0000269|PubMed:11809823}.
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, skeletal muscle and
CC brain. {ECO:0000269|PubMed:31489369, ECO:0000269|PubMed:9207786}.
CC -!- DOMAIN: The transmembrane helices are not perpendicular to the plane of
CC the membrane, but cross the membrane at an angle. Odd-numbered
CC transmembrane helices exhibit a sharp kink, due to the presence of a
CC conserved proline residue. {ECO:0000250|UniProtKB:P02722}.
CC -!- PTM: Under cell death induction, transglutaminated by TGM2
CC (PubMed:19644512). Transglutamination leads to formation of covalent
CC cross-links between a glutamine and the epsilon-amino group of a lysine
CC residue, forming polymers (PubMed:19644512).
CC {ECO:0000269|PubMed:19644512}.
CC -!- DISRUPTION PHENOTYPE: Mice display mitochondrial myopathy affecting
CC heart and skeletal muscles (PubMed:9207786). Hindlimb muscles exhibit
CC abundant ragged-red fibers, characteristic of mitochondrial myopathies
CC (PubMed:9207786). Increased mitochondrial activity is observed,
CC reflecting greater mitochondrial content (PubMed:9207786). In addition,
CC mice are exercise intolerant (PubMed:9207786). Mice develop chronic
CC progressive external ophthalmoplegia, but show normal ocular motility
CC (PubMed:16303948). In retina, while abnormalities are observed in
CC extraocular muscles, retinal structure and function are not affected
CC normal (PubMed:20671283). Cells display impaired mitochondrial
CC uncoupling (PubMed:31341297). Cells show impaired autophagy, leading to
CC accumulation of aberrant mitochondria (PubMed:31618756). Mice lacking
CC Slc25a4/Ant1 and Slc25a5/Ant2 in liver still have mitochondrial
CC permeability transition pore (mPTP) activity, although more Ca(2+) is
CC required to activate the mPTP (PubMed:14749836). Deletion of
CC Slc25a4/Ant1, Slc25a5/Ant2 and Slc25a31/Ant4 in liver completely
CC inhibits mPTP (PubMed:31489369). Mice lacking Slc25a4/Ant1,
CC Slc25a5/Ant2, Slc25a31/Ant4 and Ppif lack Ca(2+)-induced mPTP formation
CC (PubMed:31489369). {ECO:0000269|PubMed:14749836,
CC ECO:0000269|PubMed:16303948, ECO:0000269|PubMed:20671283,
CC ECO:0000269|PubMed:31341297, ECO:0000269|PubMed:31489369,
CC ECO:0000269|PubMed:31618756, ECO:0000269|PubMed:9207786}.
CC -!- SIMILARITY: Belongs to the mitochondrial carrier (TC 2.A.29) family.
CC {ECO:0000305}.
CC -!- CAUTION: Was reported as a homodimer (PubMed:11809823). However, 3D
CC structure data show that it forms a monomer (By similarity).
CC {ECO:0000250|UniProtKB:G2QNH0, ECO:0000250|UniProtKB:P02722,
CC ECO:0000269|PubMed:11809823}.
CC -!- CAUTION: It is unclear if SLC25A4/ANT1 constitutes a pore-forming
CC component of mitochondrial permeability transition pore (mPTP)
CC (PubMed:14749836, PubMed:31489369). Initial reports, based on deletion
CC of Slc25a4/Ant1 and Slc25a5/Ant2, suggested that ADP/ATP translocase
CC rather acts as a regulator of mPTP (PubMed:14749836). However, deletion
CC of all ADP/ATP translocase components (Slc25a4/Ant1, Slc25a5/Ant2 and
CC Slc25a31/Ant4) completely inhibits mPTP, suggesting that ADP/ATP
CC translocase constitutes a pore-forming component of mPTP
CC (PubMed:31489369). Discrepancy between reports may be caused by
CC overexpression of Slc25a31/Ant4 in mice lacking Slc25a4/Ant1 and
CC Slc25a5/Ant2, which compensates for the loss of Slc25a4/Ant1 and
CC Slc25a5/Ant2 (PubMed:31489369). {ECO:0000269|PubMed:14749836,
CC ECO:0000269|PubMed:31489369}.
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DR EMBL; U27315; AAC52837.1; -; mRNA.
DR EMBL; X74510; CAA52616.1; -; mRNA.
DR EMBL; AF240002; AAF64470.1; -; Genomic_DNA.
DR EMBL; BC003791; AAH03791.1; -; mRNA.
DR EMBL; BC026925; AAH26925.1; -; mRNA.
DR CCDS; CCDS40333.1; -.
DR PIR; S37210; S37210.
DR RefSeq; NP_031476.3; NM_007450.4.
DR AlphaFoldDB; P48962; -.
DR SMR; P48962; -.
DR BioGRID; 198105; 49.
DR IntAct; P48962; 18.
DR MINT; P48962; -.
DR STRING; 10090.ENSMUSP00000034049; -.
DR iPTMnet; P48962; -.
DR PhosphoSitePlus; P48962; -.
DR SwissPalm; P48962; -.
DR EPD; P48962; -.
DR jPOST; P48962; -.
DR MaxQB; P48962; -.
DR PaxDb; P48962; -.
DR PeptideAtlas; P48962; -.
DR PRIDE; P48962; -.
DR ProteomicsDB; 296118; -.
DR TopDownProteomics; P48962; -.
DR Antibodypedia; 28911; 167 antibodies from 24 providers.
DR DNASU; 11739; -.
DR Ensembl; ENSMUST00000034049; ENSMUSP00000034049; ENSMUSG00000031633.
DR GeneID; 11739; -.
DR KEGG; mmu:11739; -.
DR UCSC; uc009lpz.2; mouse.
DR CTD; 291; -.
DR MGI; MGI:1353495; Slc25a4.
DR VEuPathDB; HostDB:ENSMUSG00000031633; -.
DR eggNOG; KOG0749; Eukaryota.
DR GeneTree; ENSGT00940000154622; -.
DR HOGENOM; CLU_015166_12_0_1; -.
DR InParanoid; P48962; -.
DR OMA; YDGIVEC; -.
DR OrthoDB; 870903at2759; -.
DR PhylomeDB; P48962; -.
DR TreeFam; TF300743; -.
DR Reactome; R-MMU-83936; Transport of nucleosides and free purine and pyrimidine bases across the plasma membrane.
DR BioGRID-ORCS; 11739; 5 hits in 72 CRISPR screens.
DR ChiTaRS; Slc25a4; mouse.
DR PRO; PR:P48962; -.
DR Proteomes; UP000000589; Chromosome 8.
DR RNAct; P48962; protein.
DR Bgee; ENSMUSG00000031633; Expressed in atrioventricular valve and 259 other tissues.
DR Genevisible; P48962; MM.
DR GO; GO:0032592; C:integral component of mitochondrial membrane; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; ISO:MGI.
DR GO; GO:0045121; C:membrane raft; ISO:MGI.
DR GO; GO:0005743; C:mitochondrial inner membrane; HDA:MGI.
DR GO; GO:0005741; C:mitochondrial outer membrane; ISS:MGI.
DR GO; GO:0005757; C:mitochondrial permeability transition pore complex; IMP:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0005471; F:ATP:ADP antiporter activity; IDA:UniProtKB.
DR GO; GO:0019899; F:enzyme binding; ISO:MGI.
DR GO; GO:0017077; F:oxidative phosphorylation uncoupler activity; IDA:UniProtKB.
DR GO; GO:0015078; F:proton transmembrane transporter activity; IDA:UniProtKB.
DR GO; GO:1990845; P:adaptive thermogenesis; IMP:UniProtKB.
DR GO; GO:0015866; P:ADP transport; ISS:UniProtKB.
DR GO; GO:0008637; P:apoptotic mitochondrial changes; IGI:MGI.
DR GO; GO:0140021; P:mitochondrial ADP transmembrane transport; IDA:UniProtKB.
DR GO; GO:1990544; P:mitochondrial ATP transmembrane transport; IDA:UniProtKB.
DR GO; GO:0010667; P:negative regulation of cardiac muscle cell apoptotic process; ISO:MGI.
DR GO; GO:1902109; P:negative regulation of mitochondrial membrane permeability involved in apoptotic process; ISO:MGI.
DR GO; GO:1901029; P:negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; IBA:GO_Central.
DR GO; GO:0060546; P:negative regulation of necroptotic process; ISO:MGI.
DR GO; GO:0061051; P:positive regulation of cell growth involved in cardiac muscle cell development; ISO:MGI.
DR GO; GO:1901526; P:positive regulation of mitophagy; IDA:UniProtKB.
DR GO; GO:2000277; P:positive regulation of oxidative phosphorylation uncoupler activity; ISO:MGI.
DR GO; GO:0046902; P:regulation of mitochondrial membrane permeability; IMP:UniProtKB.
DR Gene3D; 1.50.40.10; -; 1.
DR InterPro; IPR002113; ADT_euk_type.
DR InterPro; IPR002067; Mit_carrier.
DR InterPro; IPR018108; Mitochondrial_sb/sol_carrier.
DR InterPro; IPR023395; Mt_carrier_dom_sf.
DR PANTHER; PTHR45635; PTHR45635; 1.
DR Pfam; PF00153; Mito_carr; 3.
DR PRINTS; PR00927; ADPTRNSLCASE.
DR PRINTS; PR00926; MITOCARRIER.
DR SUPFAM; SSF103506; SSF103506; 1.
DR PROSITE; PS50920; SOLCAR; 3.
PE 1: Evidence at protein level;
KW Acetylation; Antiport; Direct protein sequencing; Membrane; Methylation;
KW Mitochondrion; Mitochondrion inner membrane; Phosphoprotein;
KW Reference proteome; Repeat; S-nitrosylation; Transmembrane;
KW Transmembrane helix; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT CHAIN 2..298
FT /note="ADP/ATP translocase 1"
FT /id="PRO_0000090575"
FT TOPO_DOM 2..7
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 8..37
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 38..74
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..99
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 100..109
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 110..130
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 131..178
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 179..199
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 200..210
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT TRANSMEM 211..231
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 232..273
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000305"
FT TRANSMEM 274..291
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT TOPO_DOM 292..298
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000305"
FT REPEAT 6..98
FT /note="Solcar 1"
FT REPEAT 111..201
FT /note="Solcar 2"
FT REPEAT 212..297
FT /note="Solcar 3"
FT REGION 235..240
FT /note="Important for transport activity"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOTIF 235..240
FT /note="Nucleotide carrier signature motif"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 80
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 92
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT BINDING 235
FT /ligand="ADP"
FT /ligand_id="ChEBI:CHEBI:456216"
FT /evidence="ECO:0000250|UniProtKB:P02722"
FT MOD_RES 2
FT /note="N-acetylglycine"
FT /evidence="ECO:0000250|UniProtKB:P12235"
FT MOD_RES 7
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05962"
FT MOD_RES 52
FT /note="N6,N6,N6-trimethyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q05962"
FT MOD_RES 147
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05962"
FT MOD_RES 150
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q05962"
FT MOD_RES 160
FT /note="S-nitrosocysteine"
FT /evidence="ECO:0000250|UniProtKB:Q05962"
FT MOD_RES 245
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 272
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MUTAGEN 43
FT /note="K->E: Abolished ADP:ATP antiporter activity without
FT affecting ability to regulate mitophagy; when associated
FT with E-244."
FT /evidence="ECO:0000269|PubMed:31618756"
FT MUTAGEN 90
FT /note="A->D: Abolished ability to regulate mitophagy."
FT /evidence="ECO:0000269|PubMed:31618756"
FT MUTAGEN 123
FT /note="A->D: Abolished ability to regulate mitophagy."
FT /evidence="ECO:0000269|PubMed:31618756"
FT MUTAGEN 146..147
FT /note="GK->ED: Abolished interaction with TIMM4, thereby
FT abolishing ability to regulate mitophagy."
FT /evidence="ECO:0000269|PubMed:31618756"
FT MUTAGEN 244
FT /note="R->E: Abolished ADP:ATP antiporter activity without
FT affecting ability to regulate mitophagy; when associated
FT with E-43."
FT /evidence="ECO:0000269|PubMed:31618756"
FT CONFLICT 136
FT /note="F -> L (in Ref. 1; AAC52837)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 298 AA; 32904 MW; 3A849FEAB0981462 CRC64;
MGDQALSFLK DFLAGGIAAA VSKTAVAPIE RVKLLLQVQH ASKQISAEKQ YKGIIDCVVR
IPKEQGFLSF WRGNLANVIR YFPTQALNFA FKDKYKQIFL GGVDRHKQFW RYFAGNLASG
GAAGATSLCF VYPLDFARTR LAADVGKGSS QREFNGLGDC LTKIFKSDGL KGLYQGFSVS
VQGIIIYRAA YFGVYDTAKG MLPDPKNVHI IVSWMIAQSV TAVAGLVSYP FDTVRRRMMM
QSGRKGADIM YTGTLDCWRK IAKDEGANAF FKGAWSNVLR GMGGAFVLVL YDEIKKYV
